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Database: UniProt
Entry: A0A1G6ZPT0_9ACTN
LinkDB: A0A1G6ZPT0_9ACTN
Original site: A0A1G6ZPT0_9ACTN 
ID   A0A1G6ZPT0_9ACTN        Unreviewed;       398 AA.
AC   A0A1G6ZPT0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Uncharacterized membrane-anchored protein {ECO:0000313|EMBL:SDE04570.1};
GN   ORFNames=SAMN05216270_111132 {ECO:0000313|EMBL:SDE04570.1};
OS   Glycomyces harbinensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC   Glycomyces.
OX   NCBI_TaxID=58114 {ECO:0000313|EMBL:SDE04570.1, ECO:0000313|Proteomes:UP000198949};
RN   [1] {ECO:0000313|EMBL:SDE04570.1, ECO:0000313|Proteomes:UP000198949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3516 {ECO:0000313|EMBL:SDE04570.1,
RC   ECO:0000313|Proteomes:UP000198949};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNAD01000011; SDE04570.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6ZPT0; -.
DR   STRING; 58114.SAMN05216270_111132; -.
DR   OrthoDB; 5169996at2; -.
DR   Proteomes; UP000198949; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004788; F:thiamine diphosphokinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.10240; Thiamin pyrophosphokinase, catalytic domain; 1.
DR   InterPro; IPR047795; Put_SteA-like.
DR   InterPro; IPR022215; SteA-like_C.
DR   InterPro; IPR007371; TPK_catalytic.
DR   InterPro; IPR036759; TPK_catalytic_sf.
DR   NCBIfam; NF040608; division_SteA; 1.
DR   Pfam; PF12555; SteA-like_C; 1.
DR   Pfam; PF04263; TPK_catalytic; 1.
DR   SUPFAM; SSF63999; Thiamin pyrophosphokinase, catalytic domain; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        351..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          213..247
FT                   /note="Thiamin pyrophosphokinase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF04263"
FT   DOMAIN          339..390
FT                   /note="SteA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12555"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   398 AA;  42569 MW;  B5655342AFEBD3FB CRC64;
     MRVPSLRLPG RNPEGDSSEG RLVGTARLDR RTKRLCGRLE SGDVAIIDHV DLDRVAADTL
     VGTDVAVVVN AAKSISGRYP NLGPEVLVKA GIVLIDDVGD EIFENVREGR SVAVDGGDIY
     LGDVLIGSGT VQTEESVAAD MEAAKEGLSV QLEAFAANTM EYLKRERDLL LDGVGVPDVK
     TSFNGRHALV VIRGYNYKED IDVLRPYIRE FKPVLVGVDG GADALLEAGY TPDMIVGDMD
     SVSDDALRCG AEIVVHAYAD GRAPGMERMD RLGVPAIPFP AAATSEDIAM LMADEKGAEL
     ICAVGTHVTM VEFLDKGRGG MASTFLTRLR VGGKLVDAKG VSRLYRQDMS ISALLLLIVS
     ALAAMATAVA ISTVGRSFVD VIADWWDGLL YQIQRLFS
//
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